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MFGE8 protein, human
Known as:
MFGE8
, MFG-E8 protein, human
, Breast Epithelial Antigen BA46
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Lactadherin (387 aa, ~43 kDa) is encoded by the human MFGE8 gene. This protein plays a role in cell adhesion, phagocytosis of apoptotic cells…
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National Institutes of Health
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Related topics
Related topics
11 relations
Breast Carcinoma
Cell Adhesion
EGF-Like Domain
Epithelial Cells
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Broader (2)
Milk Proteins
Surface Antigens
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2015
Highly Cited
2015
Quantitative analysis of tissue distribution of the B16BL6-derived exosomes using a streptavidin-lactadherin fusion protein and iodine-125-labeled biotin derivative after intravenous injection in…
Masaki Morishita
,
Yuki Takahashi
,
+6 authors
Y. Takakura
Journal of Pharmacy and Science
2015
Corpus ID: 25860045
We previously succeeded in the visualization of tissue distribution of B16BL6 cells-derived exosomes by labeling with Gaussia…
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Review
2009
Review
2009
Mechanisms and consequences of efferocytosis in advanced atherosclerosis
E. Thorp
,
I. Tabas
Journal of Leukocyte Biology
2009
Corpus ID: 14846972
Throughout atherosclerotic lesion development, intimal macrophages undergo apoptosis, a form of death that usually prevents…
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Review
2009
Review
2009
From Everyday to Scientific Observation: How Children Learn to Observe the Biologist’s World
Catherine Eberbach
,
K. Crowley
2009
Corpus ID: 16320060
This article explores the development of observation in scientific and everyday contexts. Fundamental to all scientific activity…
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Review
2009
Review
2009
A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.
A. Abedini
,
D. Raleigh
Protein engineering, design & selection : PEDS
2009
Corpus ID: 21877030
Amyloidogenic proteins and polypeptides can be divided into two structural classes, namely those which are flexible and are…
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Highly Cited
2005
Highly Cited
2005
Identification, Proteomic Profiling, and Origin of Ram Epididymal Fluid Exosome-Like Vesicles1
J. Gatti
,
S. Metayer
,
M. Belghazi
,
F. Dacheux
,
J. Dacheux
Biology of Reproduction
2005
Corpus ID: 8927806
Abstract Small membranous vesicles, between 25- and 75-nm diameter, were collected by high-speed centrifugation from the ram…
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Highly Cited
2004
Highly Cited
2004
Inhibitory effects of human and bovine milk constituents on rotavirus infections.
A. Kvistgaard
,
L. T. Pallesen
,
+4 authors
J. Rasmussen
Journal of Dairy Science
2004
Corpus ID: 25346145
Among etiologic agents, rotavirus is the major cause of severe dehydration diarrhea in infant mammals. In vitro and in vivo…
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Highly Cited
2003
Highly Cited
2003
Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence* 210
T. Ban
,
D. Hamada
,
K. Hasegawa
,
H. Naiki
,
Y. Goto
Journal of Biological Chemistry
2003
Corpus ID: 13189926
Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril formation. Thioflavin T (ThT) is a…
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Highly Cited
2000
Highly Cited
2000
Functional analyses of two cellular binding domains of bovine lactadherin.
Mikkel Holmen Andersen
,
Helle Graversen
,
Sergey N. Fedosov
,
Torben E. Petersen
,
Jan T. Rasmussen
Biochemistry
2000
Corpus ID: 24217249
The glycoprotein bovine lactadherin (formerly known as PAS-6/7) comprises two EGF-like domains and two C-like domains found in…
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Highly Cited
1997
Highly Cited
1997
Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis.
X. Qi
,
Carl Holt
,
David Mcnulty
,
David T. Clarke
,
Sharon Brownlow
,
Gareth R. Jones
Biochemical Journal
1997
Corpus ID: 30176121
Previous CD measurements of changes in the conformation of beta-lactoglobulin at neutral pH as a function of temperature…
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Highly Cited
1995
Highly Cited
1995
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
B. A. Schulman
,
Christina Redfield
,
Zheng-yu Peng
,
C. M. Dobson
,
P. S. Kim
Journal of Molecular Biology
1995
Corpus ID: 38433265
alpha-Lactalbumin (alpha-LA) is a two-domain, calcium-binding protein that forms one of the best studied molten globules. We…
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